Characterisation of multiple substrate-specific (d)ITP/(d)XTPase and modelling of deaminated purine nucleotide metabolism
Davies, Oluwafemi, Mendes, Pedro, Smallbone, Kieran and Malys, Naglis. (2012) Characterisation of multiple substrate-specific (d)ITP/(d)XTPase and modelling of deaminated purine nucleotide metabolism. BMB Reports , Vol.45 (No.4). pp. 259-264. ISSN 1976-6696
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To be viable, organisms possess a number of (deoxy)nucleotide phosphohydrolases, which hydrolyze these nucleotides removing them from the active NTP and dNTP pools.
Deamination of purine bases can result in accumulation of
such nucleotides as ITP, dITP, XTP and dXTP. E. coli RdgB has been characterised as a deoxyribonucleoside triphosphate pyrophosphohydrolase that can act on these nucleotides. S. cerevisiae homologue encoded by YJR069C was purified and its (d)NTPase activity was assayed using fifteen nucleotide substrates. ITP, dITP, and XTP were identified as major substrates
and kinetic parameters measured. Inhibition by ATP,
dATP and GTP were established. On the basis of experimental and published data, modelling and simulation of ITP, dITP, XTP and dXTP metabolism was performed. (d)ITP/(d)XTPase is a new example of enzyme with multiple substrate-specificity demonstrating that multispecificity is not a rare phenomenon.
|Item Type:||Journal Article|
|Subjects:||Q Science > QP Physiology|
|Divisions:||Faculty of Science > Life Sciences (2010- )|
|Library of Congress Subject Headings (LCSH):||Deamination, Purine nucleotides, Saccharomyces cerevisiae -- Physiology|
|Journal or Publication Title:||BMB Reports|
|Publisher:||Korean Society for Biochemistry and Molecular Biology|
|Page Range:||pp. 259-264|
|Access rights to Published version:||Restricted or Subscription Access|
|Funder:||Engineering and Physical Sciences Research Council (EPSRC), Biotechnology and Biological Sciences Research Council (Great Britain) (BBSRC), Seventh Framework Programme (European Commission) (FP7)|
|Grant number:||B/C008219/1 (BBSRC/EPSRC), EP/F500 009/1 (BBSRC/EPSRC), 201142 (FP7)|
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